1idy
STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE
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OverviewOverview
A small globular protein, the third repeat of the c-Myb DNA-binding, domain, which is composed of 54 amino acid residues, was engineered so as, to understand the structural uniqueness of native proteins. This small, protein has three alpha-helices that form a helix-turn-helix structure, which is maintained by the hydrophobic core with three Ile residues. One, of the mutant proteins, with two of the buried Ile (Ile-155 and Ile-181), substituted with Leu residues, showed multiple conformations, as monitored, by heteronuclear magnetic resonance spectroscopy for 13C- and 15N-labeled, proteins. The increase in the side-chain conformational entropy, caused by, changing the Ile to a Leu residue on an alpha-helix, could engender the, lack of structural uniqueness. In native proteins, the conformations of, not only the beta-branched side chains, but also those of the neighboring, bulky side chains, can be greatly restricted, depending upon the local, backbone structure.
About this StructureAbout this Structure
1IDY is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
A small engineered protein lacks structural uniqueness by increasing the side-chain conformational entropy., Furukawa K, Oda M, Nakamura H, Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13583-8. PMID:8942977
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